Structure of PDB 4ebb Chain A

Receptor sequence
>4ebbA (length=450) Species: 9606 (Homo sapiens) [Search protein sequence]
DPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGN
EGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTE
LLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPH
LVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQI
KDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYP
TDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSEHCYDIYR
LYHSCADPTGCGTGPDARAWDYQACTEINLTFASNNVTDMFPDLPFTDEL
RQRYCLDTWGVWPRPDWLLTSFWGGDLRAASNIIFSNGNLDPWAGGGIRR
NLSASVIAVTIQGGAHHLDLRASHPEDPASVVEARKLEATIIGEWVKAAR
3D structure
PDB4ebb Structures of Human DPP7 Reveal the Molecular Basis of Specific Inhibition and the Architectural Diversity of Proline-Specific Peptidases.
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.14.2: dipeptidyl-peptidase II.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN A H451 E453 H424 E426
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0070008 serine-type exopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:1905146 lysosomal protein catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005764 lysosome
GO:0005794 Golgi apparatus
GO:0031410 cytoplasmic vesicle
GO:0031982 vesicle
GO:0035578 azurophil granule lumen
GO:0043231 intracellular membrane-bounded organelle
GO:0070062 extracellular exosome

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Biological Process

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Cellular Component
External links
PDB RCSB:4ebb, PDBe:4ebb, PDBj:4ebb
PDBsum4ebb
PubMed22952628
UniProtQ9UHL4|DPP2_HUMAN Dipeptidyl peptidase 2 (Gene Name=DPP7)

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